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Conserved domains on  [gi|332271967|gb|AEE38667|]
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ATP synthase F1 beta subunit, partial [Aeromonas taiwanensis]

Protein Classification

AtpD superfamily protein( domain architecture ID 1903243)

AtpD superfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpD super family cl43008
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-166 6.30e-143

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


The actual alignment was detected with superfamily member COG0055:

Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 404.47  E-value: 6.30e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   1 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDV 79
Cdd:COG0055  163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDV 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  80 LFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDA 159
Cdd:COG0055  243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322


                 ....*..
gi 332271967 160 TVVLSRQ 166
Cdd:COG0055  323 TTVLSRK 329
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-166 6.30e-143

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 404.47  E-value: 6.30e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   1 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDV 79
Cdd:COG0055  163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDV 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  80 LFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDA 159
Cdd:COG0055  243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322


                 ....*..
gi 332271967 160 TVVLSRQ 166
Cdd:COG0055  323 TTVLSRK 329
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-166 1.17e-129

F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410877 [Multi-domain]  Cd Length: 277  Bit Score: 363.85  E-value: 1.17e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   1 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNV-----LDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD- 74
Cdd:cd01133   84 IMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDe 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  75 EGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTF 154
Cdd:cd01133  164 EGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATTF 243

                        170
                 ....*....|..
gi 332271967 155 AHLDATVVLSRQ 166
Cdd:cd01133  244 AHLDATTVLSRG 255
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-166 1.87e-128

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 367.89  E-value: 1.87e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967    1 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDV 79
Cdd:TIGR01039 160 IQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDV 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   80 LFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDA 159
Cdd:TIGR01039 240 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDA 319


                  ....*..
gi 332271967  160 TVVLSRQ 166
Cdd:TIGR01039 320 TTVLSRK 326
atpB CHL00060
ATP synthase CF1 beta subunit
 2-165 2.50e-117

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 340.48  E-value: 2.50e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   2 MELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLD-------KVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD 74
Cdd:CHL00060 179 MELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRD 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  75 EGR-DVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATT 153
Cdd:CHL00060 259 VNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATT 338

                        170
                 ....*....|..
gi 332271967 154 FAHLDATVVLSR 165
Cdd:CHL00060 339 FAHLDATTVLSR 350
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 14-166 2.20e-68

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 206.44  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   14 GYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAG 93
Cdd:pfam00006  41 DVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEAL 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332271967   94 TEVSALLGRMPSAVGYQPTLAEEMGVLQERITST--KTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:pfam00006 121 REISLALGEPPGREGYPPSVFSLLARLLERAGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRD 195
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-166 6.30e-143

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 404.47  E-value: 6.30e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   1 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDV 79
Cdd:COG0055  163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDV 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  80 LFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDA 159
Cdd:COG0055  243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322


                 ....*..
gi 332271967 160 TVVLSRQ 166
Cdd:COG0055  323 TTVLSRK 329
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-166 1.17e-129

F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410877 [Multi-domain]  Cd Length: 277  Bit Score: 363.85  E-value: 1.17e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   1 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNV-----LDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD- 74
Cdd:cd01133   84 IMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDe 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  75 EGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTF 154
Cdd:cd01133  164 EGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATTF 243

                        170
                 ....*....|..
gi 332271967 155 AHLDATVVLSRQ 166
Cdd:cd01133  244 AHLDATTVLSRG 255
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-166 1.87e-128

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 367.89  E-value: 1.87e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967    1 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDV 79
Cdd:TIGR01039 160 IQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDV 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   80 LFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDA 159
Cdd:TIGR01039 240 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDA 319


                  ....*..
gi 332271967  160 TVVLSRQ 166
Cdd:TIGR01039 320 TTVLSRK 326
atpB CHL00060
ATP synthase CF1 beta subunit
 2-165 2.50e-117

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 340.48  E-value: 2.50e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   2 MELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLD-------KVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD 74
Cdd:CHL00060 179 MELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRD 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  75 EGR-DVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATT 153
Cdd:CHL00060 259 VNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATT 338

                        170
                 ....*....|..
gi 332271967 154 FAHLDATVVLSR 165
Cdd:CHL00060 339 FAHLDATTVLSR 350
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 3-166 3.04e-80

alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.


Pssm-ID: 132348 [Multi-domain]  Cd Length: 449  Bit Score: 244.35  E-value: 3.04e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967    3 ELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDVLF 81
Cdd:TIGR03305 157 EMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEKQDVLL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   82 FVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATV 161
Cdd:TIGR03305 237 LIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASL 316


                  ....*
gi 332271967  162 VLSRQ 166
Cdd:TIGR03305 317 VLSRK 321
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 2-165 6.23e-78

RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410884 [Multi-domain]  Cd Length: 270  Bit Score: 232.73  E-value: 6.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   2 MELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLF 81
Cdd:cd19476   85 MQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLL 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  82 FVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATTFAHLDA 159
Cdd:cd19476  165 IIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFAILDG 244


                 ....*.
gi 332271967 160 TVVLSR 165
Cdd:cd19476  245 QIVLSR 250
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 14-166 2.20e-68

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 206.44  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   14 GYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAG 93
Cdd:pfam00006  41 DVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEAL 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332271967   94 TEVSALLGRMPSAVGYQPTLAEEMGVLQERITST--KTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:pfam00006 121 REISLALGEPPGREGYPPSVFSLLARLLERAGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRD 195
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 17-166 1.94e-28

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 410880 [Multi-domain]  Cd Length: 265  Bit Score: 105.72  E-value: 1.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEV 96
Cdd:cd01136   97 VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREV 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  97 SALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:cd01136  177 GLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRR 246
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
17-166 7.74e-25

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 99.12  E-value: 7.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEV 96
Cdd:PRK06820 193 VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREI 272

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  97 SALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK06820 273 GLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRR 342
PRK08149 PRK08149
FliI/YscN family ATPase;
7-166 4.91e-24

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 96.60  E-value: 4.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   7 NIAIEHSGYSVF--AGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVD 84
Cdd:PRK08149 169 NMLIEHSEADVFviGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  85 NIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLS 164
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLS 328


                 ..
gi 332271967 165 RQ 166
Cdd:PRK08149 329 RK 330
fliI PRK08972
flagellar protein export ATPase FliI;
21-166 1.16e-20

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 87.45  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  21 VGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALL 100
Cdd:PRK08972 196 VGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAV 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332271967 101 GRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK08972 276 GEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRE 343
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
4-166 1.51e-20

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 87.12  E-value: 1.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   4 LIRNIAIEhsgYSVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFV 83
Cdd:PRK06936 182 LIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLM 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  84 DNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVL 163
Cdd:PRK06936 259 DSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIIL 338


                 ...
gi 332271967 164 SRQ 166
Cdd:PRK06936 339 SRK 341
fliI PRK08472
flagellar protein export ATPase FliI;
17-166 5.48e-20

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 85.51  E-value: 5.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGERTREGNDFYHEMMESNvLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEV 96
Cdd:PRK08472 187 VVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREI 265

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332271967  97 SALLGRMPSAVGYQPTLAEEMGVLQERITSTKT-GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK08472 266 GLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRE 336
fliI PRK07721
flagellar protein export ATPase FliI;
17-166 6.74e-20

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 85.16  E-value: 6.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEV 96
Cdd:PRK07721 188 VIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREI 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  97 SALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK07721 268 GLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQ 337
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 17-166 7.70e-20

Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440771 [Multi-domain]  Cd Length: 433  Bit Score: 84.70  E-value: 7.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEV 96
Cdd:COG1157  187 VIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREI 266

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  97 SALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:COG1157  267 GLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRK 336
fliI PRK07196
flagellar protein export ATPase FliI;
21-166 5.20e-19

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 82.63  E-value: 5.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  21 VGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALL 100
Cdd:PRK07196 189 IGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSL 268

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332271967 101 GRMPSAVGYQPT-------LAEEMGvlqeriTSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK07196 269 GEPPATKGYPPSafsiiprLAESAG------NSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRK 335
fliI PRK06793
flagellar protein export ATPase FliI;
16-166 6.66e-19

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 82.33  E-value: 6.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  16 SVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTE 95
Cdd:PRK06793 185 NVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRS 264

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332271967  96 VSALLGRMPsaVGYQPTLAEE-MGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK06793 265 VDIAVKELP--IGGKTLLMESyMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRE 334
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
16-166 6.16e-18

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 79.61  E-value: 6.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  16 SVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTE 95
Cdd:PRK07594 184 NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAARE 263

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332271967  96 VSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK07594 264 IALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRR 334
fliI PRK05688
flagellar protein export ATPase FliI;
21-166 7.08e-18

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 79.39  E-value: 7.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  21 VGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALL 100
Cdd:PRK05688 202 IGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAI 281

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332271967 101 GRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK05688 282 GEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRR 349
fliI PRK07960
flagellum-specific ATP synthase FliI;
21-166 4.68e-17

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 77.13  E-value: 4.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  21 VGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALL 100
Cdd:PRK07960 209 IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAI 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332271967 101 GRMPSAVGYQPTLAEEMGVLQERITS--TKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK07960 289 GEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRR 356
fliI PRK08927
flagellar protein export ATPase FliI;
16-166 2.09e-16

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 75.40  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  16 SVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTE 95
Cdd:PRK08927 187 SVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQRE 266

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332271967  96 VSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK08927 267 IGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERA 339
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 1-166 7.92e-14

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 68.12  E-value: 7.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967    1 MMELIRNIAIEH-------SGYSVFAGVGERTREGNDFYHEMME-------SNVLDKVSLVYGQMNEPPGNRLRVALTGL 66
Cdd:PRK14698  663 MPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGI 742

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   67 TMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI-------TSTKTGSITSVQAVY 139
Cdd:PRK14698  743 TIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVS 822

                         170       180       190
                  ....*....|....*....|....*....|...
gi 332271967  140 VPADDLTDPSPATT------FAHLDATVVLSRQ 166
Cdd:PRK14698  823 PPGGDFSEPVVQNTlrvvkvFWALDADLARRRH 855
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 16-166 1.23e-13

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 67.49  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  16 SVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTE 95
Cdd:PRK09099 192 NVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQRE 271

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332271967  96 VSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:PRK09099 272 IGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSRE 342
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 17-148 1.78e-13

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 66.06  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGER----TREGNDFYH---EMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRY 89
Cdd:cd01134  106 IYVGCGERgnemAEVLEEFPElkdPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRW 185

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332271967  90 TLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT-------GSITSVQAVYVPADDLTDP 148
Cdd:cd01134  186 AEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRClgspgreGSVTIVGAVSPPGGDFSEP 251
PRK05922 PRK05922
type III secretion system ATPase; Validated
 16-138 4.79e-11

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 59.92  E-value: 4.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  16 SVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTE 95
Cdd:PRK05922 186 NVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQE 265

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 332271967  96 VSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAV 138
Cdd:PRK05922 266 VALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAI 308
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 17-166 5.17e-11

V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 410879 [Multi-domain]  Cd Length: 282  Bit Score: 59.16  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR-DEGRDVLFFVDNIYRYTLAGTE 95
Cdd:cd01135  105 VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAyEKGKHVLVILTDMTNYAEALRE 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332271967  96 VSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQ 166
Cdd:cd01135  185 VSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRD 257
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 17-166 1.02e-07

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 50.21  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRL---RVAltgLTMAE--KFrDEGRDVLFFVDNIYRYTL 91
Cdd:PRK04196 179 VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERIltpRMA---LTAAEylAF-EKGMHVLVILTDMTNYCE 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  92 AGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVPADDLTDPSPattfahlDAT-------VV 162
Cdd:PRK04196 255 ALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIV 327


                 ....
gi 332271967 163 LSRQ 166
Cdd:PRK04196 328 LSRE 331
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 17-153 2.65e-06

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 46.18  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  17 VFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR-DEGRDVLFFVDNIYRYTLAGTE 95
Cdd:PRK02118 170 ILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKE 249

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332271967  96 VSALLGRMPSAVGYQPTLAEEMGVLQERITSTK-TGSITSVQAVYVPADDLTDPSPATT 153
Cdd:PRK02118 250 ISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEdGGSITIIAVTTMPGDDVTHPVPDNT 308
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 64-148 3.48e-06

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 45.93  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  64 TGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLA-------EEMGVLqeRITSTKTGSITSVQ 136
Cdd:PRK04192 311 TGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAsrlaefyERAGRV--KTLGGEEGSVTIIG 388

                         90
                 ....*....|..
gi 332271967 137 AVYVPADDLTDP 148
Cdd:PRK04192 389 AVSPPGGDFSEP 400
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 17-153 4.08e-06

V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273410 [Multi-domain]  Cd Length: 466  Bit Score: 45.48  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   17 VFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVLFFVDNIYRYTLAGTE 95
Cdd:TIGR01040 186 VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALRE 265

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967   96 VSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATT 153
Cdd:TIGR01040 266 VSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLT 325
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 36-104 1.86e-04

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 40.67  E-value: 1.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332271967  36 MESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMP 104
Cdd:PRK13343 213 REHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPP 281
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 16-146 4.72e-04

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 39.64  E-value: 4.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332271967  16 SVFAGVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTE 95
Cdd:PTZ00185 228 SIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQ 307

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332271967  96 VSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT----GSITSVQAVYVPADDLT 146
Cdd:PTZ00185 308 ISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVT 362
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 64-104 1.51e-03

F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410876 [Multi-domain]  Cd Length: 274  Bit Score: 37.92  E-value: 1.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 332271967  64 TGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMP 104
Cdd:cd01132  148 AGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
20-74 5.97e-03

mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 36.29  E-value: 5.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332271967  20 GVGERTREGNDFYHEMMESNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD 74
Cdd:COG5239  153 GYYERFRQTYILLNRIGEKDNIAWVCLFVGLFNKEPGDTPYVANTHLPWDPKYRD 207
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 64-104 8.57e-03

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 35.81  E-value: 8.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 332271967  64 TGLTMAEKFRDEGRDVLFFVDNI------YRytlagtEVSALLGRMP 104
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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